Structure of PDB 1wox Chain A

Receptor sequence
>1woxA (length=244) Species: 1148 (Synechocystis sp. PCC 6803) [Search protein sequence]
TNLAQKLRYGTQQSHTLAENTAYMKCFLKGIVEREPFRQLLANLYYLYSA
LEAALRQHRDNEIISAIYFPELNRTDKLAEDLTYYYGPNWQQIIQPTPCA
KIYVDRLKTIAASEPELLIAHCYTRYLGDLSGGQSLKNIIRSALQLPEGE
GTAMYEFDSLPTPGDRRQFKEIYRDVLNSLPLDEATINRIVEEANYAFSL
NREVMHDLEDLIKAAIGEHTFDLLTRQDRPGSTEGHPITLMVGE
3D structure
PDB1wox Crystal structure of dimeric heme oxygenase-2 from Synechocystis sp. PCC 6803 in complex with heme.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N21 Y49 T125 R126 G129 D130 G134
Catalytic site (residue number reindexed from 1) N20 Y48 T124 R125 G128 D129 G133
Enzyme Commision number 1.14.14.18: heme oxygenase (biliverdin-producing).
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 HEM A R9 H16 E20 M25 L29 Y124 T125 L128 G129 S132 G133 F199 N202 S233 T234 G241 R8 H15 E19 M24 L28 Y123 T124 L127 G128 S131 G132 F198 N201 S232 T233 G235
BS02 NO A G129 G133 G128 G132
Gene Ontology
Molecular Function
GO:0004392 heme oxygenase (decyclizing) activity
GO:0016491 oxidoreductase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0006788 heme oxidation
GO:0006979 response to oxidative stress
GO:0015979 photosynthesis
GO:0042167 heme catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1wox, PDBe:1wox, PDBj:1wox
PDBsum1wox
PubMed15766254
UniProtP74133|HO2_SYNY3 Heme oxygenase 2 (Gene Name=pbsA2)

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